NRK_HUMAN
ID NRK_HUMAN Reviewed; 1582 AA.
AC Q7Z2Y5; Q32ND6; Q5H9K2; Q6ZMP2;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Nik-related protein kinase;
DE EC=2.7.11.1;
GN Name=NRK;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Ovary;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1291 (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-852; SER-855; SER-1027;
RP SER-1031 AND SER-1034, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [6]
RP VARIANTS [LARGE SCALE ANALYSIS] HIS-355; MET-358; CYS-424; ALA-426;
RP GLY-579; GLY-679; LEU-880; GLY-971; SER-1106; PRO-1121; LEU-1276; ALA-1471
RP AND LEU-1472.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: May phosphorylate cofilin-1 and induce actin polymerization
CC through this process, during the late stages of embryogenesis. Involved
CC in the TNF-alpha-induced signaling pathway (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7Z2Y5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z2Y5-2; Sequence=VSP_020654, VSP_020657;
CC Name=3;
CC IsoId=Q7Z2Y5-3; Sequence=VSP_020655, VSP_020656;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC protein kinase family. STE20 subfamily. {ECO:0000305}.
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DR EMBL; BX538345; CAD98108.1; -; mRNA.
DR EMBL; Z68339; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z69734; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z70274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z83850; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC108702; AAI08703.1; -; mRNA.
DR EMBL; AK131549; BAD18683.1; -; mRNA.
DR CCDS; CCDS65305.1; -. [Q7Z2Y5-1]
DR RefSeq; NP_940867.2; NM_198465.3. [Q7Z2Y5-1]
DR AlphaFoldDB; Q7Z2Y5; -.
DR SMR; Q7Z2Y5; -.
DR BioGRID; 128472; 3.
DR IntAct; Q7Z2Y5; 2.
DR STRING; 9606.ENSP00000434830; -.
DR GlyGen; Q7Z2Y5; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q7Z2Y5; -.
DR PhosphoSitePlus; Q7Z2Y5; -.
DR BioMuta; NRK; -.
DR DMDM; 115502506; -.
DR jPOST; Q7Z2Y5; -.
DR MassIVE; Q7Z2Y5; -.
DR PaxDb; Q7Z2Y5; -.
DR PeptideAtlas; Q7Z2Y5; -.
DR PRIDE; Q7Z2Y5; -.
DR ProteomicsDB; 68985; -. [Q7Z2Y5-1]
DR ProteomicsDB; 68986; -. [Q7Z2Y5-2]
DR ProteomicsDB; 68987; -. [Q7Z2Y5-3]
DR Antibodypedia; 2074; 65 antibodies from 21 providers.
DR DNASU; 203447; -.
DR Ensembl; ENST00000243300.14; ENSP00000434830.1; ENSG00000123572.17. [Q7Z2Y5-1]
DR Ensembl; ENST00000536164.5; ENSP00000438785.1; ENSG00000123572.17. [Q7Z2Y5-3]
DR GeneID; 203447; -.
DR KEGG; hsa:203447; -.
DR MANE-Select; ENST00000243300.14; ENSP00000434830.1; NM_198465.4; NP_940867.2.
DR UCSC; uc065ans.1; human. [Q7Z2Y5-1]
DR CTD; 203447; -.
DR DisGeNET; 203447; -.
DR GeneCards; NRK; -.
DR HGNC; HGNC:25391; NRK.
DR HPA; ENSG00000123572; Tissue enhanced (adrenal gland, ovary, placenta).
DR MIM; 300791; gene.
DR neXtProt; NX_Q7Z2Y5; -.
DR OpenTargets; ENSG00000123572; -.
DR PharmGKB; PA134869113; -.
DR VEuPathDB; HostDB:ENSG00000123572; -.
DR eggNOG; KOG0587; Eukaryota.
DR GeneTree; ENSGT00940000161533; -.
DR HOGENOM; CLU_001831_2_0_1; -.
DR InParanoid; Q7Z2Y5; -.
DR OrthoDB; 533537at2759; -.
DR PhylomeDB; Q7Z2Y5; -.
DR PathwayCommons; Q7Z2Y5; -.
DR SignaLink; Q7Z2Y5; -.
DR BioGRID-ORCS; 203447; 23 hits in 714 CRISPR screens.
DR ChiTaRS; NRK; human.
DR GeneWiki; NRK_(gene); -.
DR GenomeRNAi; 203447; -.
DR Pharos; Q7Z2Y5; Tdark.
DR PRO; PR:Q7Z2Y5; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q7Z2Y5; protein.
DR Bgee; ENSG00000123572; Expressed in tibia and 121 other tissues.
DR ExpressionAtlas; Q7Z2Y5; baseline and differential.
DR Genevisible; Q7Z2Y5; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00036; CNH; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50219; CNH; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1582
FT /note="Nik-related protein kinase"
FT /id="PRO_0000250511"
FT DOMAIN 25..313
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 1209..1552
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT REGION 492..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 783..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 926..1156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 725..759
FT /evidence="ECO:0000255"
FT COMPBIAS 492..514
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..560
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..813
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 820..859
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 926..942
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 943..977
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1019
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1065
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1136..1156
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 177
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 31..39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 54
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1027
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1031
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 1034
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..332
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020654"
FT VAR_SEQ 164..188
FT /note="GLAHLHAHRVIHRDIKGQNVLLTHN -> PKVIFLGTGCSDSSLKKELCLKH
FT QN (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020655"
FT VAR_SEQ 189..1582
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020656"
FT VAR_SEQ 333..338
FT /note="IIKKRQ -> MFFSFV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020657"
FT VARIANT 355
FT /note="Q -> H (in dbSNP:rs55862725)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040951"
FT VARIANT 358
FT /note="V -> M (in dbSNP:rs209373)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_033908"
FT VARIANT 424
FT /note="S -> C (in a breast infiltrating ductal carcinoma
FT sample; somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040952"
FT VARIANT 426
FT /note="P -> A (in dbSNP:rs55635933)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040953"
FT VARIANT 579
FT /note="E -> G (in dbSNP:rs56350428)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040954"
FT VARIANT 679
FT /note="E -> G (in dbSNP:rs35115195)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040955"
FT VARIANT 727
FT /note="R -> H (in dbSNP:rs33936206)"
FT /id="VAR_051653"
FT VARIANT 880
FT /note="I -> L (in a colorectal adenocarcinoma sample;
FT somatic mutation; dbSNP:rs764355898)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040956"
FT VARIANT 971
FT /note="D -> G (in dbSNP:rs35334892)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040957"
FT VARIANT 993
FT /note="A -> E (in dbSNP:rs16984889)"
FT /id="VAR_033909"
FT VARIANT 1106
FT /note="P -> S (in dbSNP:rs35393519)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040958"
FT VARIANT 1121
FT /note="A -> P (in dbSNP:rs35720774)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040959"
FT VARIANT 1276
FT /note="H -> L (in dbSNP:rs35942881)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040960"
FT VARIANT 1471
FT /note="G -> A (in dbSNP:rs34232354)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040961"
FT VARIANT 1472
FT /note="M -> L (in dbSNP:rs35609510)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040962"
FT CONFLICT 152
FT /note="D -> G (in Ref. 1; CAD98108)"
FT /evidence="ECO:0000305"
FT CONFLICT 522
FT /note="G -> S (in Ref. 1; CAD98108)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="E -> G (in Ref. 1; CAD98108)"
FT /evidence="ECO:0000305"
FT CONFLICT 705
FT /note="R -> G (in Ref. 1; CAD98108)"
FT /evidence="ECO:0000305"
FT CONFLICT 1138
FT /note="S -> P (in Ref. 1; CAD98108)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1582 AA; 178479 MW; C9C56860C8AEBFF3 CRC64;
MAGPGGWRDR EVTDLGHLPD PTGIFSLDKT IGLGTYGRIY LGLHEKTGAF TAVKVMNARK
TPLPEIGRRV RVNKYQKSVG WRYSDEEEDL RTELNLLRKY SFHKNIVSFY GAFFKLSPPG
QRHQLWMVME LCAAGSVTDV VRMTSNQSLK EDWIAYICRE ILQGLAHLHA HRVIHRDIKG
QNVLLTHNAE VKLVDFGVSA QVSRTNGRRN SFIGTPYWMA PEVIDCDEDP RRSYDYRSDV
WSVGITAIEM AEGAPPLCNL QPLEALFVIL RESAPTVKSS GWSRKFHNFM EKCTIKNFLF
RPTSANMLQH PFVRDIKNER HVVESLTRHL TGIIKKRQKK GIPLIFEREE AIKEQYTVRR
FRGPSCTHEL LRLPTSSRCR PLRVLHGEPS QPRWLPDREE PQVQALQQLQ GAARVFMPLQ
ALDSAPKPLK GQAQAPQRLQ GAARVFMPLQ AQVKAKASKP LQMQIKAPPR LRRAARVLMP
LQAQVRAPRL LQVQSQVSKK QQAQTQTSEP QDLDQVPEEF QGQDQVPEQQ RQGQAPEQQQ
RHNQVPEQEL EQNQAPEQPE VQEQAAEPAQ AETEAEEPES LRVNAQVFLP LLSQDHHVLL
PLHLDTQVLI PVEGQTEGSP QAQAWTLEPP QAIGSVQALI EGLSRDLLRA PNSNNSKPLG
PLQTLMENLS SNRFYSQPEQ AREKKSKVST LRQALAKRLS PKRFRAKSSW RPEKLELSDL
EARRQRRQRR WEDIFNQHEE ELRQVDKDKE DESSDNDEVF HSIQAEVQIE PLKPYISNPK
KIEVQERSPS VPNNQDHAHH VKFSSSVPQR SLLEQAQKPI DIRQRSSQNR QNWLAASESS
SEEESPVTGR RSQSSPPYST IDQKLLVDIH VPDGFKVGKI SPPVYLTNEW VGYNALSEIF
RNDWLTPAPV IQPPEEDGDY VELYDASADT DGDDDDESND TFEDTYDHAN GNDDLDNQVD
QANDVCKDHD DDNNKFVDDV NNNYYEAPSC PRASYGRDGS CKQDGYDGSR GKEEAYRGYG
SHTANRSHGG SAASEDNAAI GDQEEHAANI GSERRGSEGD GGKGVVRTSE ESGALGLNGE
ENCSETDGPG LKRPASQDFE YLQEEPGGGN EASNAIDSGA APSAPDHESD NKDISESSTQ
SDFSANHSSP SKGSGMSADA NFASAILYAG FVEVPEESPK QPSEVNVNPL YVSPACKKPL
IHMYEKEFTS EICCGSLWGV NLLLGTRSNL YLMDRSGKAD ITKLIRRRPF RQIQVLEPLN
LLITISGHKN RLRVYHLTWL RNKILNNDPE SKRRQEEMLK TEEACKAIDK LTGCEHFSVL
QHEETTYIAI ALKSSIHLYA WAPKSFDEST AIKVCIDQSA DSEGDYMSYQ AYIRILAKIQ
AADPVNRFKR PDELLHLLKL KVFPTLDHKP VTVDLAIGSE KRLKIFFSSA DGYHLIDAES
EVMSDVTLPK NPLEIIIPQN IIILPDCLGI GMMLTFNAEA LSVEANEQLF KKILEMWKDI
PSSIAFECTQ RTTGWGQKAI EVRSLQSRVL ESELKRRSIK KLRFLCTRGD KLFFTSTLRN
HHSRVYFMTL GKLEELQSNY DV
